Sequence analysis of tyrosine recombinases allows annotation of mobile genetic elements in prokaryotic genomes [PDF]
Molecular Systems Biology, 2021 Mobile genetic elements (MGEs) sequester and mobilize antibiotic resistance genes across bacterial genomes. Efficient and reliable identification of such elements is necessary to follow resistance spreading.
Georgy Smyshlyaev +2 more
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Archaeal tyrosine recombinases. [PDF]
FEMS Microbiol Rev, 2021 ABSTRACTThe integration of mobile genetic elements into their host chromosome influences the immediate fate of cellular organisms and gradually shapes their evolution. Site-specific recombinases catalyzing this integration have been extensively characterized both in bacteria and eukarya.
Badel C, Da Cunha V, Oberto J.
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Starships are active eukaryotic transposable elements mobilized by a new family of tyrosine recombinases. [PDF]
Proc Natl Acad Sci U S A, 2023 Transposable elements in eukaryotic organisms have historically been considered “selfish,” at best conferring indirect benefits to their host organisms. The Starships are a recently discovered feature in fungal genomes that are, in some cases, predicted to confer beneficial traits to their ...
Urquhart AS +3 more
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Genome engineering in Bacillus anthracis using tyrosine site-specific recombinases. [PDF]
PLoS ONE, 2017 Tyrosine site-specific recombinases (T-SSR) are polynucleotidyltransferases that catalyze cutting and joining reactions between short specific DNA sequences. We developed three systems for performing genetic modifications in Bacillus anthracis that use T-
Andrei P Pomerantsev +5 more
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In vitro DNA Inversions Mediated by the PsrA Site-Specific Tyrosine Recombinase of Streptococcus pneumoniae [PDF]
Frontiers in Molecular Biosciences, 2020 Site-specific recombination is a DNA breaking and reconstructing process that plays important roles in various cellular pathways for both prokaryotes and eukaryotes. This process requires a site-specific recombinase and direct or inverted repeats.
Jingwen Li +5 more
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Conversion of a telomere resolvase into a Cre-like site-specific recombinase. [PDF]
PLoS ONEHairpin telomere resolvases are a unique family of enzymes involved in producing the hairpin (hp) telomeres of bacterial organisms and phages that possess linear DNA's terminated by hp telomeres.
Shu Hui Huang +2 more
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Towards a more accurate annotation of tyrosine-based site-specific recombinases in bacterial genomes [PDF]
Mobile DNA, 2012 Background Tyrosine-based site-specific recombinases (TBSSRs) are DNA breaking-rejoining enzymes. In bacterial genomes, they play a major role in the comings and goings of mobile genetic elements (MGEs), such as temperate phage genomes, integrated ...
Van Houdt Rob +4 more
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Structure of yeast kinetochore Ndc10 DNA-binding domain reveals unexpected evolutionary relationship to tyrosine recombinases. [PDF]
J Biol Chem, 2012 We have solved the x-ray structure of the N-terminal half of the yeast kinetochore protein Ndc10 at 1.9 Å resolution. This essential protein is a key constituent of the budding yeast centromere and is essential for the recruitment of the centromeric nucleosome and establishment of the kinetochore.
Perriches T, Singleton MR.
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Integrase-associated niche differentiation of endogenous large DNA viruses in crustaceans [PDF]
Microbiology SpectrumCrustacean genomes harbor sequences originating from nimaviruses, a family of large double-stranded DNA viruses infecting crustaceans. In this study, we recovered metagenome-assembled genomes of 27 endogenous nimaviruses from crustacean genome data ...
Satoshi Kawato +3 more
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New peptide inhibitors of type IB topoisomerases: similarities and differences vis-a-vis inhibitors of tyrosine recombinases. [PDF]
J Mol Biol, 2006 Topoisomerases relieve topological tension in DNA by breaking and rejoining DNA phosphodiester bonds. Type IB topoisomerases such as vaccinia topoisomerase (vTopo) and human topoisomerase I are structurally and mechanistically similar to the tyrosine recombinase family of enzymes, which includes bacteriophage lambda Integrase (Int).
Fujimoto DF, Pinilla C, Segall AM.
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